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1ava

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[[Image:1ava.gif|left|200px]]
 
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{{Structure
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==AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED==
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|PDB= 1ava |SIZE=350|CAPTION= <scene name='initialview01'>1ava</scene>, resolution 1.90&Aring;
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<StructureSection load='1ava' size='340' side='right'caption='[[1ava]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACA:Active+Site'>ACA</scene> and <scene name='pdbsite=ACB:Active+Site'>ACB</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1ava]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVA FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ava FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ava OCA], [https://pdbe.org/1ava PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ava RCSB], [https://www.ebi.ac.uk/pdbsum/1ava PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ava ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMY2_HORVU AMY2_HORVU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1ava_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ava ConSurf].
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<div style="clear:both"></div>
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'''AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED'''
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Barley alpha-amylase is a 45 kDa enzyme which is involved in starch degradation during barley seed germination. The released sugars provide the plant embryo with energy for growth. The major barley alpha-amylase isozyme (AMY2) binds with high affinity to the endogenous inhibitor BASI (barley alpha-amylase/subtilisin inhibitor) whereas the minor isozyme (AMY1) is not inhibited. BASI is a 19.6 kDa bifunctional protein that can simultaneously inhibit AMY2 and serine proteases of the subtilisin family. This inhibitor may therefore prevent degradation of the endosperm starch during premature sprouting and protect the seed from attack by pathogens secreting proteases. RESULTS: The crystal structure of AMY2 in complex with BASI was determined and refined at 1.9 A resolution. BASI consists of a 12-stranded beta-barrel structure which belongs to the beta-trefoil fold family and inhibits AMY2 by sterically occluding access of the substrate to the active site of the enzyme. The AMY2-BASI complex is characterized by an unusual completely solvated calcium ion located at the protein-protein interface. CONCLUSIONS: The AMY2-BASI complex represents the first reported structure of an endogenous protein-protein complex from a higher plant. The structure of the complex throws light on the strict specificity of BASI for AMY2, and shows that domain B of AMY2 contributes greatly to the specificity of enzyme-inhibitor recognition. In contrast to the three-dimensional structures of porcine pancreatic alpha-amylase in complex with proteinaceous inhibitors, the AMY2-BASI structure reveals that the catalytically essential amino acid residues of the enzyme are not directly bound to the inhibitor. Binding of BASI to AMY2 creates a cavity, exposed to the external medium, that is ideally shaped to accommodate an extra calcium ion. This feature may contribute to the inhibitory effect, as the key amino acid sidechains of the active site are in direct contact with water molecules which are in turn ligated to the calcium ion.
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==About this Structure==
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1AVA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVA OCA].
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==Reference==
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Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution., Vallee F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R, Structure. 1998 May 15;6(5):649-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9634702 9634702]
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[[Category: Alpha-amylase]]
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bourne, Y.]]
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[[Category: Bourne Y]]
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[[Category: Haser, R.]]
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[[Category: Haser R]]
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[[Category: Juy, M.]]
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[[Category: Juy M]]
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[[Category: Kadziola, A.]]
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[[Category: Kadziola A]]
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[[Category: Svensson, B.]]
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[[Category: Svensson B]]
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[[Category: Vallee, F.]]
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[[Category: Vallee F]]
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[[Category: CA]]
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[[Category: enzyme inhibitor complex]]
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[[Category: hydrolase inhibition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:40 2008''
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Current revision

AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED

PDB ID 1ava

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